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2-methylcitrate synthase (2-MCS) (mcs) (EC 2.3.3.5) ((2S,3S)-2-methylcitrate synthase) (Citrate synthase) (EC 2.3.3.16)

 PRPC_SALTY              Reviewed;         389 AA.
Q56063;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
23-JAN-2002, sequence version 2.
07-NOV-2018, entry version 114.
RecName: Full=2-methylcitrate synthase {ECO:0000303|PubMed:10482501};
Short=2-MCS {ECO:0000303|PubMed:20970504};
Short=mcs {ECO:0000303|PubMed:10482501};
EC=2.3.3.5 {ECO:0000269|PubMed:10482501, ECO:0000269|PubMed:20970504};
AltName: Full=Citrate synthase {ECO:0000303|PubMed:10482501};
EC=2.3.3.16 {ECO:0000269|PubMed:10482501, ECO:0000269|PubMed:20970504};
Name=prpC {ECO:0000303|PubMed:9006051}; OrderedLocusNames=STM0369;
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Salmonella.
NCBI_TaxID=99287;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=LT2 / SGSC1412 / ATCC 700720;
PubMed=9006051; DOI=10.1128/jb.179.3.928-940.1997;
Horswill A.R., Escalante-Semerena J.C.;
"Propionate catabolism in Salmonella typhimurium LT2: two divergently
transcribed units comprise the prp locus at 8.5 centisomes, prpR
encodes a member of the sigma-54 family of activators, and the prpBCDE
genes constitute an operon.";
J. Bacteriol. 179:928-940(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=LT2 / SGSC1412 / ATCC 700720;
PubMed=11677609; DOI=10.1038/35101614;
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M.,
Waterston R., Wilson R.K.;
"Complete genome sequence of Salmonella enterica serovar Typhimurium
LT2.";
Nature 413:852-856(2001).
[3]
FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL
PROPERTIES, SUBSTRATE SPECIFICITY, AND SUBUNIT.
PubMed=10482501;
Horswill A.R., Escalante-Semerena J.C.;
"Salmonella typhimurium LT2 catabolizes propionate via the 2-
methylcitric acid cycle.";
J. Bacteriol. 181:5615-5623(1999).
[4]
X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, AND SUBUNIT.
PubMed=20970504; DOI=10.1016/j.jsb.2010.10.008;
Chittori S., Savithri H.S., Murthy M.R.;
"Crystal structure of Salmonella typhimurium 2-methylcitrate synthase:
Insights on domain movement and substrate specificity.";
J. Struct. Biol. 174:58-68(2011).
-!- FUNCTION: Involved in the catabolism of short chain fatty acids
(SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route)
and via the 2-methylcitrate cycle I (propionate degradation
route). Catalyzes the Claisen condensation of propionyl-CoA and
oxaloacetate (OAA) to yield 2-methylcitrate (2-MC) and CoA. Also
catalyzes the condensation of oxaloacetate with acetyl-CoA or
butyryl-CoA but with a lower specificity.
{ECO:0000269|PubMed:10482501, ECO:0000269|PubMed:20970504}.
-!- CATALYTIC ACTIVITY: Propanoyl-CoA + H(2)O + oxaloacetate =
(2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate + CoA.
{ECO:0000269|PubMed:10482501, ECO:0000269|PubMed:20970504}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + H(2)O + oxaloacetate = citrate +
CoA. {ECO:0000269|PubMed:10482501, ECO:0000269|PubMed:20970504}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=12 uM for oxaloacetate (with propionyl-CoA)
{ECO:0000269|PubMed:10482501};
KM=13 uM for oxaloacetate (with propionyl-CoA at pH 8 and 30
degrees Celsius) {ECO:0000269|PubMed:20970504};
KM=14 uM for oxaloacetate (with acetyl-CoA)
{ECO:0000269|PubMed:10482501};
KM=15 uM for oxaloacetate (with acetyl-CoA at pH 8 and 30
degrees Celsius) {ECO:0000269|PubMed:20970504};
KM=45 uM for propionyl-CoA (at pH 8 and 30 degrees Celsius)
{ECO:0000269|PubMed:20970504};
KM=48 uM for propionyl-CoA {ECO:0000269|PubMed:10482501};
KM=265 uM for acetyl-CoA (at pH 8 and 30 degrees Celsius)
{ECO:0000269|PubMed:20970504};
KM=285 uM for acetyl-CoA {ECO:0000269|PubMed:10482501};
Vmax=2 umol/min/mg enzyme with acetyl-CoA as substrate
{ECO:0000269|PubMed:10482501};
Vmax=2.5 umol/min/mg enzyme with acetyl-CoA as substrate (at pH
8 and 30 degrees Celsius) {ECO:0000269|PubMed:20970504};
Vmax=10 umol/min/mg enzyme with propionyl-CoA as substrate
{ECO:0000269|PubMed:10482501};
Vmax=11 umol/min/mg enzyme with propionyl-CoA as substrate (at
pH 8 and 30 degrees Celsius) {ECO:0000269|PubMed:20970504};
Note=Kcat is 1.4 sec(-1) for citrate synthase activity with
acetyl-CoA as substrate. Kcat is 1.87 sec(-1) for citrate
synthase activity with acetyl-CoA as substrate (at pH 8 and 30
degrees Celsius). Kcat is 7.4 sec(-1) for 2-methylcitrate
synthase activity with propionyl-CoA as substrate. Kcat is 8.25
sec(-1) for 2-methylcitrate synthase activity with propionyl-CoA
as substrate (at pH 8 and 30 degrees Celsius).
{ECO:0000269|PubMed:10482501, ECO:0000269|PubMed:20970504};
-!- PATHWAY: Organic acid metabolism; propanoate degradation.
{ECO:0000305|PubMed:9006051}.
-!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
isocitrate from oxaloacetate: step 1/2.
{ECO:0000305|PubMed:9006051}.
-!- SUBUNIT: Homodimer at low concentrations and converted to a larger
oligomers at higher concentrations. {ECO:0000269|PubMed:10482501,
ECO:0000269|PubMed:20970504}.
-!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to
accumulate propionyl-CoA. {ECO:0000269|PubMed:10482501}.
-!- SIMILARITY: Belongs to the citrate synthase family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U51879; AAC44815.1; -; Genomic_DNA.
EMBL; AE006468; AAL19323.1; -; Genomic_DNA.
RefSeq; NP_459364.1; NC_003197.2.
RefSeq; WP_000132749.1; NC_003197.2.
PDB; 3O8J; X-ray; 2.41 A; A/B/C/D/E/F/G/H/I/J=1-389.
PDBsum; 3O8J; -.
ProteinModelPortal; Q56063; -.
SMR; Q56063; -.
STRING; 99287.STM0369; -.
PaxDb; Q56063; -.
PRIDE; Q56063; -.
EnsemblBacteria; AAL19323; AAL19323; STM0369.
GeneID; 1251888; -.
KEGG; stm:STM0369; -.
PATRIC; fig|99287.12.peg.391; -.
eggNOG; ENOG4105BZN; Bacteria.
eggNOG; COG0372; LUCA.
HOGENOM; HOG000021225; -.
KO; K01659; -.
OMA; NFLWMTF; -.
PhylomeDB; Q56063; -.
BioCyc; MetaCyc:MONOMER-63; -.
BioCyc; SENT99287:G1FZD-374-MONOMER; -.
BRENDA; 2.3.3.5; 5542.
UniPathway; UPA00223; UER00717.
UniPathway; UPA00946; -.
EvolutionaryTrace; Q56063; -.
Proteomes; UP000001014; Chromosome.
GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
GO; GO:0050440; F:2-methylcitrate synthase activity; IDA:UniProtKB.
GO; GO:0004108; F:citrate (Si)-synthase activity; IBA:GO_Central.
GO; GO:0036440; F:citrate synthase activity; IDA:UniProtKB.
GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; IDA:UniProtKB.
GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
Gene3D; 1.10.230.10; -; 1.
Gene3D; 1.10.580.10; -; 1.
InterPro; IPR011278; 2-MeCitrate/Citrate_synth_II.
InterPro; IPR016142; Citrate_synth-like_lrg_a-sub.
InterPro; IPR016143; Citrate_synth-like_sm_a-sub.
InterPro; IPR002020; Citrate_synthase.
InterPro; IPR019810; Citrate_synthase_AS.
InterPro; IPR024176; Citrate_synthase_bac-typ.
InterPro; IPR036969; Citrate_synthase_sf.
PANTHER; PTHR11739; PTHR11739; 1.
Pfam; PF00285; Citrate_synt; 1.
PIRSF; PIRSF001369; Citrate_synth; 1.
PRINTS; PR00143; CITRTSNTHASE.
SUPFAM; SSF48256; SSF48256; 1.
TIGRFAMs; TIGR01800; cit_synth_II; 1.
PROSITE; PS00480; CITRATE_SYNTHASE; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Reference proteome; Transferase;
Tricarboxylic acid cycle.
CHAIN 1 389 2-methylcitrate synthase.
/FTId=PRO_0000169982.
REGION 268 272 Coenzyme A binding.
{ECO:0000250|UniProtKB:O34002}.
ACT_SITE 235 235 {ECO:0000250|UniProtKB:O34002,
ECO:0000305|PubMed:20970504}.
ACT_SITE 274 274 {ECO:0000250|UniProtKB:O34002,
ECO:0000305|PubMed:20970504}.
ACT_SITE 325 325 {ECO:0000250|UniProtKB:O34002,
ECO:0000305|PubMed:20970504}.
BINDING 82 82 Substrate.
{ECO:0000250|UniProtKB:I6Y9Q3}.
BINDING 200 200 Substrate.
{ECO:0000250|UniProtKB:I6Y9Q3}.
BINDING 283 283 Substrate.
{ECO:0000250|UniProtKB:I6Y9Q3}.
BINDING 350 350 Substrate.
{ECO:0000250|UniProtKB:I6Y9Q3}.
BINDING 369 369 Substrate.
{ECO:0000250|UniProtKB:I6Y9Q3}.
CONFLICT 144 144 S -> N (in Ref. 1; AAC44815).
{ECO:0000305}.
STRAND 29 35 {ECO:0000244|PDB:3O8J}.
STRAND 42 44 {ECO:0000244|PDB:3O8J}.
HELIX 49 55 {ECO:0000244|PDB:3O8J}.
HELIX 58 66 {ECO:0000244|PDB:3O8J}.
STRAND 67 69 {ECO:0000244|PDB:3O8J}.
HELIX 73 84 {ECO:0000244|PDB:3O8J}.
HELIX 91 98 {ECO:0000244|PDB:3O8J}.
HELIX 106 120 {ECO:0000244|PDB:3O8J}.
HELIX 129 156 {ECO:0000244|PDB:3O8J}.
HELIX 169 178 {ECO:0000244|PDB:3O8J}.
HELIX 184 196 {ECO:0000244|PDB:3O8J}.
STRAND 201 203 {ECO:0000244|PDB:3O8J}.
HELIX 204 213 {ECO:0000244|PDB:3O8J}.
TURN 214 216 {ECO:0000244|PDB:3O8J}.
HELIX 219 230 {ECO:0000244|PDB:3O8J}.
TURN 233 235 {ECO:0000244|PDB:3O8J}.
HELIX 238 246 {ECO:0000244|PDB:3O8J}.
HELIX 252 264 {ECO:0000244|PDB:3O8J}.
HELIX 282 298 {ECO:0000244|PDB:3O8J}.
HELIX 302 318 {ECO:0000244|PDB:3O8J}.
TURN 324 326 {ECO:0000244|PDB:3O8J}.
HELIX 327 334 {ECO:0000244|PDB:3O8J}.
HELIX 339 341 {ECO:0000244|PDB:3O8J}.
HELIX 342 363 {ECO:0000244|PDB:3O8J}.
STRAND 372 374 {ECO:0000244|PDB:3O8J}.
HELIX 385 387 {ECO:0000244|PDB:3O8J}.
SEQUENCE 389 AA; 43173 MW; 0927008F1E5F38D4 CRC64;
MTDTTILQNN THVIKPKKSV ALSGVPAGNT ALCTVGKSGN DLHYRGYDIL DLAEHCEFEE
VAHLLIHGKL PTRDELNAYK SKLKALRGLP ANVRTVLEAL PAASHPMDVM RTGVSALGCT
LPEKEGHTVS GARDIADKLL ASLSSILLYW YHYSHNGERI QPETDDDSIG GHFLHLLHGE
KPTQSWEKAM HISLVLYAEH EFNASTFTSR VIAGTGSDVY SAIIGAIGAL RGPKHGGANE
VSLEIQQRYE TPDEAEADIR KRVENKEVVI GFGHPVYTIA DPRHQVIKRV AKQLSEEGGS
LKMYHIADRL ETVMWETKKM FPNLDWFSAV SYNMMGVPTE MFTPLFVIAR VTGWAAHIIE
QRQDNKIIRP SANYTGPEDR PFVSIDDRC


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